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Safety Information

SAB4200357

Sigma-Aldrich

Anti-Profilin 1 antibody, Mouse monoclonal

clone Profilin 1-3, purified from hybridoma cell culture

Synonym(s):

Anti-PFN1

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About This Item

UNSPSC Code:
12352203
NACRES:
NA.41

biological source

mouse

conjugate

unconjugated

antibody form

purified from hybridoma cell culture

antibody product type

primary antibodies

clone

Profilin 1-3, monoclonal

form

buffered aqueous solution

mol wt

antigen ~15 kDa

species reactivity

rat, bovine, human, mouse, canine

concentration

~1.0 mg/mL

technique(s)

immunoprecipitation (IP): suitable
western blot: 1-2 μg/mL using whole extracts of HeLa or NRK cells

isotype

IgG1

UniProt accession no.

shipped in

dry ice

storage temp.

−20°C

target post-translational modification

unmodified

Gene Information

human ... PFN1(5216)
mouse ... Pfn1(18643)
rat ... Pfn1(64303)

General description

Monoclonal Anti-Profilin 1 (mouse IgG1 isotype) is derived from the hybridoma Profilin1-3 produced by the fusion of mouse myeloma cells and splenocytes from BALB/c mice immunized with a synthetic peptide corresponding to a sequence located near the C-terminus of human profiling 1, conjugated to keyhole limpet hemocyanin (KLH). Profilin-1 (Pfn1), a major actin-regulatory protein is mapped to human chromosome17p13. It is the most ubiquitous and abundant protein and is highly expressed throughout development and adulthood in most tissues including brain.

Immunogen

synthetic peptide corresponding to a sequence located near the C-terminus of human profilin 1, conjugated to KLH. The corresponding sequence is identical in mouse and rat profilin 1.

Application

Monoclonal Anti-Profilin 1 antibody produced in mouse has been used in immunoblotting and immunoprecipitation.

Biochem/physiol Actions

Profilin-1 (Pfn1) is involved in actin polymerization in response to extracellular signals. Profilins were shown to be important for normal cell proliferation, differentiation and motility. Profilin 1 is a potent regulator of actin filament dynamics. It is suggested to act as a tumor suppressor protein based on its reduced expression in several types of invasive cancers and its ability to suppress tumorigenicity when over expressed in breast cancer cells. Deletion of the profilin 1 gene leads to an embryonic lethal phenotype.

Physical form

Solution in 0.01 M phosphate buffered saline, pH 7.4, containing 15 mM sodium azide.

Disclaimer

Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.

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Storage Class Code

10 - Combustible liquids

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable


Regulatory Listings

Regulatory Listings are mainly provided for chemical products. Only limited information can be provided here for non-chemical products. No entry means none of the components are listed. It is the user’s obligation to ensure the safe and legal use of the product.

JAN Code

SAB4200357-BULK:
SAB4200357-VAR:
SAB4200357-200UL:


Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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A balanced level of profilin-1 promotes stemness and tumor-initiating potential of breast cancer cells
Jiang C, et al.
Cell Cycle, 16(24) (2017)
PFN1 mutations are rare in Han Chinese populations with amyotrophic lateral sclerosis
Chen YP, et al.
Neurobiology of Aging, 34(7) (2013)
Structure and functions of profilins
Krishnan K, et al.
Biophysical Reviews, 1(2), 71-71 (2009)
Profilin I is essential for cell survival and cell division in early mouse development
Witke W, et al.
Proceedings of the National Academy of Sciences of the USA, 98(7), 3832-3836 (2001)
Sung Haeng Lee et al.
Molecules and cells, 29(4), 311-325 (2010-05-07)
The dynamic remolding of the actin cytoskeleton is a critical part of most cellular activities, and malfunction of cytoskeletal proteins results in various human diseases. The transition between two forms of actin, monomeric or G-actin and filamentous or F-actin, is

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